Protein Degradation in Development and Aging
Our laboratory uses the nematode worm Caenorhabditis elegans as a model organismn to study general regulatory aspects of the ubiquitin/proteasome system (UPS) in developmental and aging processes. We currently have one Postdoc or two PhD positions available and are looking for outstanding candidates. Candidates should ideally already have been exposed to a laboratory environment. While previous experience in C. elegans is not necessary, this, or experience with a genetic system would certainly be a plus.
Selected Literature:
The ubiquitin-selective chaperone CDC-48/p97 links myosin assembly to human myopathy.
Janiesch P.C., Kim J., Mouysset J., Barikbin R., Lochmüller H., Cassata G., Krause S., and Hoppe T. (2007). Nat. Cell Biol. (doi: 10.1038/ncb1554)
The UNC-45 Chaperone Mediates Sarcomere Assembly through Myosin Degradation in C. elegans. Landsverk M.L., Hutagalung A.H., Li S., Najafov A., Hoppe T., Barral J.M., and Epstein H.F. (2007).
J. Cell Biol. (in press)
A Conserved Role of C. elegans CDC-48 in ER-Associated Protein Degradation.
Mouysset J., Kähler C., and Hoppe T. (2006). Journal Struct. Biol. 156, 41-49.
Multiubiquitylation by E4 enzymes: one size doesn’t fit all.
Hoppe T. (2005). Trends Biochem. Sci. 30, 183-187.
Regulation of the Myosin-Directed Chaperone UNC-45 by a Novel E3/E4-Multiubiquitylation Complex in C. elegans. Hoppe T., Cassata G., Barral J.M., Springer W., Hutagalung A.H., Epstein H.F., and Baumeister R. (2004). Cell 118, 337-49.
To apply, please forward curriculum vitae, bibliography, and the names and addresses of referees to:
Dr. Thorsten Hoppe, Centre for Molecular Neurobiology Hamburg (ZMNH), Falkenried 94, 20251 Hamburg, Germany,
thorsten.hoppe AT zmnh.uni-hamburg.de